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Immunological crossreactivity of G-protein beta subunit and receptors for activated C-kinase
M Robles-Flores1, J A García-Sáinz
1Departamento de Bioenergética, Facultad de Medicina, Universidad Nacional Autónoma de México, México D. F.
Selective antisera against: 1) RACKs, 2) a putative common PKC-binding domain (peptide I), and 3) G-protein subunits, were used for immunoblot analysis with recombinant purified beta 1 gamma 2 subunits and a crude preparation of RACKs. Antipeptide I recognized not only RACKs but also the G-protein beta subunit. In addition, two RACK-specific antisera immunoreacted with the G-protein beta subunit. Similarly, anti-G beta comm and S-217 (beta gamma-specific antiserum) crossreacted with RACKs. Using an overlay assay, it was observed that proteins immunoprecipitated with anti-RACKs or with anti-G beta antisera bound activated PKC.
Selective antisera against: 1) RACKs, 2) a putative common PKC-binding domain (peptide I), and 3) G-protein subunits, were used for immunoblot analysis with recombinant purified beta 1 gamma 2 subunits and a crude preparation of RACKs. Antipeptide I recognized not only RACKs but also the G-protein beta subunit. In addition, two RACK-specific antisera immunoreacted with the G-protein beta subunit. Similarly, anti-G beta comm and S-217 (beta gamma-specific antiserum) crossreacted with RACKs. Using an overlay assay, it was observed that proteins immunoprecipitated with anti-RACKs or with anti-G beta antisera bound activated PKC.